ApoList – November 2021


Caspases and IAPs


Caspase-2 regulates S-phase cell cycle events to protect from DNA damage accumulation independent of apoptosis – Ashley G. Boice, Karla E. Lopez, Raj K. Pandita, Melissa J. Parsons, Chloe I. Charendoff, Vijay Charaka, Alexandre F. Carisey, Tej K. Pandita and Lisa Bouchier-Hayes. https://www.nature.com/articles/s41388-021-02085-w
XIAP restrains TNF-driven intestinal inflammation and dysbiosis by promoting innate immune responses of Paneth and dendritic cells – Adam Wahida, Madeleine Müller, Andreas Hiergeist, Bastian Popper, Katja Steiger, Caterina Branca, Markus Tschurtschenthaler, Thomas Engleitner, Sainitin Donakonda, Jordy De Coninck, Rupert Öllinger, Marie K. Pfautsch, Nicole Müller, Miguel Silva, Sinem Usluer, Erik Thiele Oberg, Jan P. Böttcher, Nicole Pfarr, Martina Anton, Julia B. Slotta-Huspenina, Andreas G. Nerlich, Tobias Madl, Marijana Basic, André Bleich, Geert Berx, Jürgen Ruland, Percy A. Knolle, Roland Rad, Timon E. Adolph, Peter Vandenabeele, Hirokazu Kanegane, André Gessner, Philipp J. Jost, Monica Yabal. https://www.science.org/doi/full/10.1126/sciimmunol.abf7235
Deficiency in X-linked inhibitor of apoptosis protein promotes susceptibility to microbial triggers of intestinal inflammation – Anne Strigli, Shreya Gopalakrishnan, Yvonne Zeissig, Marijana Basic, Jun Wang, Tobias Schwerd, Shauni Doms, Kenneth Peuker, Jelka Hartwig, Jürgen Harder, Pia Hönscheid, Philipp Arnold, Thomas Kurth, Fabian Rost, Britt-Sabina Petersen, Michael Forster, Andre Franke, Judith R. Kelsen, Meino Rohlfs, Christoph Klein, Aleixo M. Muise, Neil Warner, Ryusuke Nambu, Julia Mayerle, Helga-Paula Török, Andreas Linkermann, Michael H. Muders, Gustavo B. Baretton, Jochen Hampe, Daniela E. Aust, John F. Baines, André Bleich, Sebastian Zeissig. https://www.science.org/doi/full/10.1126/sciimmunol.abf7473
SMAC/Diablo controls proliferation of cancer cells by regulating phosphatidylethanolamine synthesis – Swaroop Kumar Pandey, Avijit Paul, Anna Shteinfer-Kuzmine, Ran Zalk, Uwe Bunz, Varda Shoshan-Barmatz. https://febs.onlinelibrary.wiley.com/doi/full/10.1002/1878-0261.12959


Efferocytosis, entosis, cell-cell


Apoptotic stress-induced FGF signalling promotes non-cell autonomous resistance to cell death – Florian J. Bock, Egor Sedov, Elle Koren, Anna L. Koessinger, Catherine Cloix, Désirée Zerbst, Dimitris Athineos, Jayanthi Anand, Kirsteen J. Campbell, Karen Blyth, Yaron Fuchs and Stephen W. G. Tait. https://www.nature.com/articles/s41467-021-26613-0
TRAIL signaling promotes entosis in colorectal cancer – Emir Bozkurt; Heiko Düssmann; Manuela Salvucci; Brenton L. Cavanagh ; Sandra Van Schaeybroeck; Daniel B. Longley; Seamus J. Martin; Jochen H.M. Prehn. https://rupress.org/jcb/article-abstract/220/11/e202010030/212649
Human intestinal and circulating invariant natural killer T cells are cytotoxic against colorectal cancer cells via the perforin–granzyme pathway – Angélica Díaz-Basabe, Claudia Burrello, Georgia Lattanzi, Fiorenzo Botti, Alberto Carrara, Elisa Cassinotti, Flavio Caprioli, Federica Facciotti. https://febs.onlinelibrary.wiley.com/doi/full/10.1002/1878-0261.13104


Death receptors


HOIP limits anti‐tumor immunity by protecting against combined TNF and IFN‐gamma‐induced apoptosis – Andrew J Freeman, Stephin J Vervoort, Jessica Michie, Kelly M Ramsbottom, John Silke, Conor J Kearney, Jane Oliaro. https://www.embopress.org/doi/abs/10.15252/embr.202153391
A patch of positively charged residues regulates the efficacy of clinical DR5 antibodies in solid tumors – Gururaj Shivange, Tanmoy Mondal, Evan Lyerly, Sanchita Bhatnagar, Charles N. Landen, Shivani Reddy, Jonathan Kim, Britney Doan, Paula Riddle, Jogender Tushir-Singh. https://www.cell.com/cell-reports/fulltext/S2211-1247(21)01430-3
A comprehensive interaction study provides a potential domain interaction network of human death domain superfamily proteins – Wei Zhou, Naoe Kaneko, Tomoya Nakagita, Hiroyuki Takeda and Junya Masumoto. https://www.nature.com/articles/s41418-021-00796-x
TRAIL/DR5 pathway promotes AKT phosphorylation, skeletal muscle differentiation, and glucose uptake – Barbara Toffoli, Federica Tonon, Veronica Tisato, Giorgio Zauli, Paola Secchiero, Bruno Fabris and Stella Bernardi. https://www.nature.com/articles/s41419-021-04383-3


Necroptosis, RIP kinases, MLKL


Oligomerization‐driven MLKL ubiquitylation antagonizes necroptosis – Zikou Liu, Laura F Dagley, Kristy Shield-Artin, Samuel N Young, Aleksandra Bankovacki, Xiangyi Wang, Michelle Tang, Jason Howitt, Che A Stafford, Ueli Nachbur, Cheree Fitzgibbon, Sarah E Garnish, Andrew I Webb, David Komander, James M Murphy, Joanne M Hildebrand, John Silke. https://www.embopress.org/doi/abs/10.15252/embj.2019103718
Human RIPK3 maintains MLKL in an inactive conformation prior to cell death by necroptosis – Yanxiang Meng, Katherine A. Davies and James M. Murphy. https://www.nature.com/articles/s41467-021-27032-x
MLKL promotes cellular differentiation in myeloid leukemia by facilitating the release of G-CSF – Xin Wang, Uris Ros, Deepti Agrawal, Eva C. Keller, Julia Slotta-Huspenina, Veronika Dill, Bo Shen, Run Shi, Tobias Herold, Claus Belka, Ritu Mishra, Florian Bassermann, Ana J. Garcia-Saez and Philipp J. Jost. https://www.nature.com/articles/s41418-021-00811-1
Caspase‐9 acts as a regulator of necroptotic cell death – Tamás Molnár, Petra Pallagi, Bálint Tél, Róbert Király, Eszter Csoma, Viktória Jenei, Zsófia Varga, Péter Gogolák, Anne Odile Hueber, Zoltán Máté, Ferenc Erdélyi, Gábor Szabó, Aladár Pettkó-Szandtner, Attila Bácsi, László Virág, József Maléth, Gábor Koncz. https://febs.onlinelibrary.wiley.com/doi/full/10.1111/febs.15898
Quantitative analysis of phosphoproteome in necroptosis reveals a role of TRIM28 phosphorylation in promoting necroptosis-induced cytokine production – Rui Zu, Zhen Yu, Jing Zhao, Xiaojuan Lu, Wei Liang, Le Sun, Chenfang Si, Kezhou Zhu, Tian Zhang, Ganquan Li, Mengmeng Zhang, Yaoyang Zhang, Nan Liu, Junying Yuan and Bing Shan. https://www.nature.com/articles/s41419-021-04290-7
Genetic inhibition of RIPK3 ameliorates functional outcome in controlled cortical impact independent of necroptosis – Limin Wu, Joon Yong Chung, Tian Cao, Gina Jin, William J. Edmiston III, Suzanne Hickman, Emily S. Levy, Jordyn A. Whalen, Eliza Sophie LaRovere Abrams, Alexei Degterev, Eng H. Lo, Lorenzo Tozzi, David L. Kaplan, Joseph El Khoury and Michael J. Whalen. https://www.nature.com/articles/s41419-021-04333-z
Proteomic analysis of necroptotic extracellular vesicles – Inbar Shlomovitz, Ziv Erlich, Gali Arad, Liat Edry-Botzer, Sefi Zargarian, Hadar Cohen, Tal Manko, Yifat Ofir-Birin, Tomer Cooks, Neta Regev-Rudzki and Motti Gerlic. https://www.nature.com/articles/s41419-021-04317-z


Reviews


Molecular mechanisms and functions of pyroptosis in inflammation and antitumor immunity – Junwei Hou, Jung-Mao Hsu, Mien-Chie Hung. https://www.cell.com/molecular-cell/fulltext/S1097-2765(21)00737-1
Soluble CD95L in cancers and chronic inflammatory disorders, a new therapeutic target? – Keerthi Kurma, Andrea Boizard-Moracchini, Gael Galli, Mickael Jean, Pierre Vacher, Patrick Blanco, Patrick Legembre. https://www.sciencedirect.com/science/article/abs/pii/S0304419X21000937
First we eat, then we do everything else: The dynamic metabolic regulation of efferocytosis – Alissa Trzeciak, Ya-Ting Wang, Justin Shaun Arnold Perry. https://www.cell.com/cell-metabolism/fulltext/S1550-4131(21)00364-8
Apoptotic cell-derived metabolites in efferocytosis-mediated resolution of inflammation – Yiwei Mao. https://www.sciencedirect.com/science/article/abs/pii/S1359610121000745
Dying cells fan the flames of inflammation – Kim Newton, Vishva M. Dixit, Nobuhiko Kayagaki. https://www.science.org/doi/10.1126/science.abi5934#.YaAPliOd4NI


Comments


Cell death leaves a new TRAIL – Michael Overholtzer. https://rupress.org/jcb/article/220/11/e202109018/212699
In Conversation with Tony Letai – Eleni Skourti, Anthony Letai. https://febs.onlinelibrary.wiley.com/doi/full/10.1111/febs.16229
Editor Profile: Eli Arama. https://febs.onlinelibrary.wiley.com/doi/full/10.1111/febs.15902
Bcl-xL and IP3R interaction: Intimate relationship with an uncertain outcome – Nikolay Popgeorgieva, Germain Gillet. https://www.sciencedirect.com/science/article/abs/pii/S0143416021001585


Bcl-2 family proteins


Bcl-xL acts as an inhibitor of IP3R channels, thereby antagonizing Ca2+-driven apoptosis – Nicolas Rosa, Hristina Ivanova, Larry E. Wagner 2nd, Justin Kale, Rita La Rovere, Kirsten Welkenhuyzen, Nikolaos Louros, Spyridoula Karamanou, Victoria Shabardina, Irma Lemmens, Elien Vandermarliere, Kozo Hamada, Hideaki Ando, Frederic Rousseau, Joost Schymkowitz, Jan Tavernier, Katsuhiko Mikoshiba, Anastassios Economou, David W. Andrews, Jan B. Parys, David I. Yule and Geert Bultynck. https://www.nature.com/articles/s41418-021-00894-w
BH3-only proteins Puma and Beclin1 regulate autophagic death in neurons in response to Amyloid-β – Akash Saha, Suraiya Saleem, Paidi Ramesh Kumar and Subhas C. Biswas. https://www.nature.com/articles/s41420-021-00748-x
The BAX-binding protein MOAP1 associates with LC3 and promotes closure of the phagophore – Hao-Chun Chang, Ran N. Tao, Chong Teik Tan, Ya Jun Wu, Boon Huat Bay and Victor C. Yu. https://www.tandfonline.com/doi/full/10.1080/15548627.2021.1896157
Venetoclax imparts distinct cell death sensitivity and adaptivity patterns in T cells – Lindsey M. Ludwig, Katrina M. Hawley, David B. Banks, Anika T. Thomas-Toth, Bruce R. Blazar, Megan E. McNerney, Joel D. Leverson and James L. LaBelle. https://www.nature.com/articles/s41419-021-04285-4
Development of a BCL-xL and BCL-2 dual degrader with improved anti-leukemic activity – Dongwen Lv, Pratik Pal, Xingui Liu, Yannan Jia, Dinesh Thummuri, Peiyi Zhang, Wanyi Hu, Jing Pei, Qi Zhang, Shuo Zhou, Sajid Khan, Xuan Zhang, Nan Hua, Qingping Yang, Sebastian Arango, Weizhou Zhang, Digant Nayak, Shaun K. Olsen, Susan T. Weintraub, Robert Hromas, Marina Konopleva, Yaxia Yuan, Guangrong Zheng and Daohong Zhou. https://www.nature.com/articles/s41467-021-27210-x
Paradoxical implication of BAX/BAK in the persistence of tetraploid cells – Jiayin Deng, Lucía G. Gutiérrez, Gautier Stoll, Omar Motiño, Isabelle Martins, Lucía Núñez, José Manuel Bravo-San Pedro, Juliette Humeau, Chloé Bordenave, Juncheng Pan, Hélène Fohrer-Ting, Sylvie Souquere, Gerard Pierron, Claudio Hetz, Carlos Villalobos, Guido Kroemer and Laura Senovilla. https://www.nature.com/articles/s41419-021-04321-3
UBQLN4 is an ATM substrate that stabilizes the anti‐apoptotic proteins BCL2A1 and BCL2L10 in mesothelioma – Fang Liu, RunSang Pan, HongYu Ding, LiLing Gu, Yun Yang, ChuanYin Li, YongJie Xu, Ronggui Hu, Hui Chen, XiangYan Zhang, YingJie Nie. https://febs.onlinelibrary.wiley.com/doi/full/10.1002/1878-0261.13058
BAX mitochondrial integration is regulated allosterically by its α1−α2 loop – Michael A. Dengler, Leonie Gibson and Jerry M. Adams. https://www.nature.com/articles/s41418-021-00815-x


Pyroptosis


Gasdermin D mediates host cell death bu not interleukin-1β secretion in Mycobacterium tuberculosis-infected macrophages – Sebastian J. Theobald, Jessica Gräb, Melanie Fritsch, Isabelle Suárez, Hannah S. Eisfeld, Sandra Winter, Maximilian Koch, Christoph Hölscher, Manolis Pasparakis, Hamid Kashkar and Jan Rybniker. https://www.nature.com/articles/s41420-021-00716-5

ApoList – November 2018

http://eepurl.com/cvmBlv


Efferocytosis / Inflammation


The Mitochondrial Apoptotic Effectors BAX/BAK Activate Caspase-3 and -7 to Trigger NLRP3 Inflammasome and Caspase-8 Driven IL-1β Activation – James E. Vince, Dominic De Nardo, Wenqing Gao, Angelina J. Vince, Cathrine Hall, Kate McArthur, Daniel Simpson, Swarna Vijayaraj, Lisa M. Lindqvist, Philippe Bouillet, Mark A. Rizzacasa, Si Ming Man, John Silke, Seth L. Masters, Guillaume Lessene, David C.S. Huang, Daniel H.D. Gray, Benjamin T. Kile, Feng Shao, Kate E. Lawlor. https://www.cell.com/cell-reports/fulltext/S2211-1247(18)31725-X

BAX/BAK-Induced Apoptosis Results in Caspase-8-Dependent IL-1β Maturation in Macrophages – Dhruv Chauhan, Eva Bartok, Moritz M. Gaidt, Florian J. Bock, Jennifer Herrmann, Jens M. Seeger, Petr Broz, Roland Beckmann, Hamid Kashkar, Stephen W.G. Tait, Rolf Müller, Veit Hornung. https://www.cell.com/cell-reports/fulltext/S2211-1247(18)31691-7

Efferocytosis induces a novel SLC program to promote glucose uptake and lactate release – Sho Morioka, Justin S. A. Perry, Michael H. Raymond, Christopher B. Medina, Yunlu Zhu, Liyang Zhao, Vlad Serbulea, Suna Onengut-Gumuscu, Norbert Leitinger, Sarah Kucenas, Jeffrey C. Rathmell, Liza Makowski and Kodi S. Ravichandran. https://www.nature.com/articles/s41586-018-0735-5

Efferocytosis of apoptotic alveolar epithelial cells is sufficient to initiate lung fibrosis – Kevin K. Kim, Megan R. Dotson, Manisha Agarwal, Jibing Yang, Patrick B. Bradley, Natalia Subbotina, John J. Osterholzer and Thomas H. Sisson. https://www.nature.com/articles/s41419-018-1074-z


Pyroptosis / Gasdermin D / Gasdermin E


Caspase-8 induces cleavage of gasdermin D to elicit pyroptosis during Yersinia infection – Joseph Sarhan, Beiyun C. Liu, Hayley I. Muendlein, Peng Li, Rachael Nilson, Amy Y. Tang, Anthony Rongvaux, Stephen C. Bunnell, Feng Shao, Douglas R. Green, and Alexander Poltorak. http://www.pnas.org/content/115/46/E10888?etoc=

Pathogen blockade of TAK1 triggers caspase-8–dependent cleavage of gasdermin D and cell death – Pontus Orning, Dan Weng, Kristian Starheim, Dmitry Ratner, Zachary Best, Bettina Lee, Alexandria Brooks, Shiyu Xia, Hao Wu, Michelle A. Kelliher, Scott B. Berger, Peter J. Gough, John Bertin, Megan M. Proulx, Jon D. Goguen, Nobuhiko Kayagaki, Katherine A. Fitzgerald, Egil Lien. http://science.sciencemag.org/content/362/6418/1064

ESCRT-dependent membrane repair negatively regulates pyroptosis downstream of GSDMD activation – Sebastian Rühl, Kateryna Shkarina, Benjamin Demarco, Rosalie Heilig, José Carlos Santos, Petr Broz. http://science.sciencemag.org/content/362/6417/956

Shiga Toxin/Lipopolysaccharide Activates Caspase-4 and Gasdermin D to Trigger Mitochondrial Reactive Oxygen Species Upstream of the NLRP3 Inflammasome – Jaye M. Platnich, Hyunjae Chung, Arthur Lau, Christina F. Sandall, Adom Bondzi-Simpson, Huey-Miin Chen, Takanori Komada, Aaron C. Trotman-Grant, Jeremy R. Brandelli, Justin Chun, Paul L. Beck, Dana J. Philpott, Stephen E. Girardin, May Ho, Roger P. Johnson, Justin A. MacDonald, Glen D. Armstrong, Daniel A. Muruve. https://www.cell.com/cell-reports/fulltext/S2211-1247(18)31531-6

Molecular Targeted Therapies Elicit Concurrent Apoptotic and GSDME-Dependent Pyroptotic Tumor Cell Death – Haijiao Lu, Shengzhe Zhang, Jie Wu, Minjiang Chen, Mei-Chun Cai, Yujie Fu, Wenfeng Li, Jing Wang, Xiaojing Zhao, Zhuang Yu, Pengfei Ma and Guanglei Zhuang. http://clincancerres.aacrjournals.org/content/24/23/6066

Gasdermin E Does Not Limit Apoptotic Cell Disassembly by Promoting Early Onset of Secondary Necrosis in Jurkat T Cells and THP-1 Monocytes – Rochelle Tixeira, Bo Shi†, Michael A. F. Parkes, Amy L. Hodge, Sarah Caruso, Mark D. Hulett, Amy A. Baxter, Thanh Kha Phan and Ivan K. H. Poon. https://www.frontiersin.org/articles/10.3389/fimmu.2018.02842/full


Death receptors / FLIP


TBK1 and IKKε prevent TNF-induced cell death by RIPK1 phosphorylation – Elodie Lafont, Peter Draber, Eva Rieser, Matthias Reichert, Sebastian Kupka, Diego de Miguel, Helena Draberova, Anne von Mässenhausen, Amandeep Bhamra, Stephen Henderson, Katarzyna Wojdyla, Avigayil Chalk, Silvia Surinova, Andreas Linkermann and Henning Walczak. https://www.nature.com/articles/s41556-018-0229-6

Fas receptor induces apoptosis of synovial bone and cartilage progenitor populations and promotes bone loss in antigen-induced arthritis – Elvira Lazić Mosler, Nina Lukač, Darja Flegar, Martina Fadljević, Igor Radanović, Hrvoje Cvija, Tomislav Kelava, Sanja Ivčević, Alan Šućur, Antonio Markotić, Vedran Katavić, Ana Marušić, Danka Grčević and Nataša Kovačić. https://www.fasebj.org/doi/abs/10.1096/fj.201801426R?ai=ts&ui=ly8&af=T

Cell polarity and adherens junction formation inhibit epithelial Fas cell death receptor signaling – Laurent Gagnoux-Palacios, Hala Awina, Stéphane Audebert, Aurélie Rossin, Magali Mondin, Franck Borgese, Carlota Planas-Botey, Amel Mettouchi, Jean-Paul Borg and Anne-Odile Hueber. http://jcb.rupress.org/content/217/11/3839?etoc

Cytoplasmic FLIP(S) and nuclear FLIP(L) mediate resistance of castrate-resistant prostate cancer to apoptosis induced by IAP antagonists – Christopher McCann, Nyree Crawford, Joanna Majkut, Caitriona Holohan, Chris W. D. Armstrong, Pamela J. Maxwell, Chee Wee Ong, Melissa J. LaBonte, Simon S. McDade, David J. Waugh and Daniel B. Longley. https://www.nature.com/articles/s41419-018-1125-5


Mcl-1


A Novel MCL1 Inhibitor Combined with Venetoclax Rescues Venetoclax-Resistant Acute Myelogenous Leukemia – Haley E. Ramsey, Melissa A. Fischer, Taekyu Lee, Agnieszka E. Gorska, Maria Pia Arrate, Londa Fuller, Kelli L. Boyd, Stephen A. Strickland, John Sensintaffar, Leah J. Hogdal, Gregory D. Ayers, Edward T. Olejniczak, Stephen W. Fesik and Michael R. Savona. http://cancerdiscovery.aacrjournals.org/content/8/12/1566

AMG 176, a Selective MCL1 Inhibitor, Is Effective in Hematologic Cancer Models Alone and in Combination with Established Therapies – Sean Caenepeel, Sean P. Brown, Brian Belmontes, Gordon Moody, Kathleen S. Keegan, Danny Chui, Douglas A. Whittington, Xin Huang, Leszek Poppe, Alan C. Cheng, Mario Cardozo, Jonathan Houze, Yunxiao Li, Brian Lucas, Nick A. Paras, Xianghong Wang, Joshua P. Taygerly, Marc Vimolratana, Manuel Zancanella, Liusheng Zhu, Elaina Cajulis, Tao Osgood, Jan Sun, Leah Damon, Regina K. Egan, Patricia Greninger, Joseph D. McClanaghan, Jianan Gong, Donia Moujalled, Giovanna Pomilio, Pedro Beltran, Cyril H. Benes, Andrew W. Roberts, David C. Huang, Andrew Wei, Jude Canon, Angela Coxon and Paul E. Hughes. http://cancerdiscovery.aacrjournals.org/content/8/12/1582

Exploiting MCL1 Dependency with Combination MEK + MCL1 Inhibitors Leads to Induction of Apoptosis and Tumor Regression in KRAS-Mutant Non–Small Cell Lung Cancer – Varuna Nangia, Faria M. Siddiqui, Sean Caenepeel, Daria Timonina, Samantha J. Bilton, Nicole Phan, Maria Gomez-Caraballo, Hannah L. Archibald, Chendi Li, Cameron Fraser, Diamanda Rigas, Kristof Vajda, Lorin A. Ferris, Michael Lanuti, Cameron D. Wright, Kevin A. Raskin, Daniel P. Cahill, John H. Shin, Colleen Keyes, Lecia V. Sequist, Zofia Piotrowska, Anna F. Farago, Christopher G. Azzoli, Justin F. Gainor, Kristopher A. Sarosiek, Sean P. Brown, Angela Coxon, Cyril H. Benes, Paul E. Hughes and Aaron N. Hata. http://cancerdiscovery.aacrjournals.org/content/8/12/1598

Increased Synthesis of MCL-1 Protein Underlies Initial Survival of EGFR-Mutant Lung Cancer to EGFR Inhibitors and Provides a Novel Drug Target – Kyung-A Song, Yasuyuki Hosono, Crystal Turner, Sheeba Jacob, Timothy L. Lochmann, Yoshiko Murakami, Neha U. Patel, Jungoh Ham, Bin Hu, Krista M. Powell, Colin M. Coon, Brad E. Windle, Yuko Oya, Jennifer E. Koblinski, Hisashi Harada, Joel D. Leverson, Andrew J. Souers, Aaron N. Hata, Sosipatros Boikos, Yasushi Yatabe, Hiromichi Ebi and Anthony C. Faber. http://clincancerres.aacrjournals.org/content/24/22/5658

Survival of midbrain dopamine neurons depends on the Bcl2 factor Mcl1 – Edward J. Robinson, Sebastian P. Aguiar, Willemieke M. Kouwenhoven, Dorinde S. Starmans, Lars von Oerthel et al. https://www.nature.com/articles/s41420-018-0125-7


Other Bcl-2 family proteins


VDAC2 enables BAX to mediate apoptosis and limit tumor development – Hui San Chin, Mark X. Li, Iris K. L. Tan, Robert L. Ninnis, Boris Reljic, Kristen Scicluna, Laura F. Dagley, Jarrod J. Sandow, Gemma L. Kelly, Andre L. Samson, Stephane Chappaz, Seong L. Khaw, Catherine Chang, Andrew Morokoff, Kerstin Brinkmann, Andrew Webb, Colin Hockings, Cathrine M. Hall, Andrew J. Kueh, Michael T. Ryan, Ruth M. Kluck, Philippe Bouillet, Marco J. Herold, Daniel H. D. Gray, David C. S. Huang, Mark F. van Delft and Grant Dewson. https://www.nature.com/articles/s41467-018-07309-4

Mannose impairs tumour growth and enhances chemotherapy – Pablo Sierra Gonzalez, James O’Prey, Simone Cardaci, Valentin J. A. Barthet, Jun-ichi Sakamaki, Florian Beaumatin, Antonia Roseweir, David M. Gay, Gillian Mackay, Gaurav Malviya, Elżbieta Kania, Shona Ritchie, Alice D. Baudot, Barbara Zunino, Agata Mrowinska, Colin Nixon, Darren Ennis, Aoisha Hoyle, David Millan, Iain A. McNeish, Owen J. Sansom, Joanne Edwards and Kevin M. Ryan. https://www.nature.com/articles/s41586-018-0729-3

Venetoclax with azacitidine disrupts energy metabolism and targets leukemia stem cells in patients with acute myeloid leukemia – Daniel A. Pollyea, Brett M. Stevens[…], Craig T. Jordan. https://www.nature.com/articles/s41591-018-0233-1

And the companion paper:
Inhibition of Amino Acid Metabolism Selectively Targets Human Leukemia Stem Cells – Courtney L. Jones, Brett M. Stevens, Angelo D’Alessandro, Julie A. Reisz, Rachel Culp-Hill, Travis Nemkov, Shanshan Pei, Nabilah Khan, Biniam Adane, Haobin Ye, Anna Krug, Dominik Reinhold, Clayton Smith, James DeGregori, Daniel A. Pollyea, Craig T. Jordan. https://www.cell.com/cancer-cell/fulltext/S1535-6108(18)30471-9

Tamoxifen overrides autophagy inhibition in Beclin-1-deficient glioma cells and their resistance to adenovirus-mediated oncolysis via upregulation of PUMA and BAX – Natalya V. Kaverina, Zaira G. Kadagidze, Anton V. Borovjagin, Apollon I. Karseladze, Chung Kwon Kim, Maciej S. Lesniak, Jason Miska, Peng Zhang, Maria A. Baryshnikova, Ting Xiao, David Ornelles, Charles Cobbs, Andrey Khramtsov and Ilya V. Ulasov. https://www.nature.com/articles/s41388-018-0395-9

NOXA genetic amplification or pharmacologic induction primes lymphoma cells to BCL2 inhibitor-induced cell death – Yuxuan Liu, Patrizia Mondello, Tatiana Erazo, Neeta Bala Tannan, Zahra Asgari, Elisa de Stanchina, Gouri Nanjangud, Venkatraman E. Seshan, Shenqiu Wang, Hans-Guido Wendel and Anas Younes. http://www.pnas.org/content/115/47/12034?etoc=

Cytoplasmic pro-apoptotic function of the tumor suppressor p73 is mediated through a modified mode of recognition of the anti-apoptotic regulator Bcl-XL – Mi-Kyung Yoon, Bu-Yeon Kim, Ji-Young Lee, Ji-Hyang Ha, Sung Ah Kim, Dong-Hwa Lee, Min-Sung Lee, Mi-Kyung Lee, Jin Sun Choi, Jin Hwa Cho, Jeong-Hoon Kim, Sunhong Kim, Jaewhan Song, Sung Goo Park, Byoung Chul Park, Kwang-Hee Bae, Sang Un Choi and Seung-Wook Chi. http://www.jbc.org/content/early/2018/11/14/jbc.RA118.003061.abstract


Caspases


Caspases maintain tissue integrity by an apoptosis-independent inhibition of cell migration and invasion – Anna Gorelick-Ashkenazi, Ron Weiss, Lena Sapozhnikov, Anat Florentin, Lama Tarayrah-Ibraheim, Dima Dweik, Keren Yacobi-Sharon and Eli Arama. https://www.nature.com/articles/s41467-018-05204-6

Identification of a novel caspase cleavage site in huntingtin that regulates mutant huntingtin clearance – Dale D. O. Martin, Mandi E. Schmidt, Yen T. Nguyen, Nikola Lazic and Michael R. Hayden. https://www.fasebj.org/doi/abs/10.1096/fj.201701510RRR?ai=ts&ui=ly8&af=T

14‐3‐3 protein masks the nuclear localization sequence of caspase‐2 – Aneta Smidova, Miroslava Alblova, Dana Kalabova, Katarina Psenakova, Michal Rosulek, Petr Herman, Tomas Obsil, Veronika Obsilova. https://febs.onlinelibrary.wiley.com/doi/10.1111/febs.14670

Tri-arginine exosite patch of caspase-6 recruits substrates for hydrolysis – Derek J MacPherson, Caityln L Mills, Mary Jo Ondrechen and Jeanne A. Hardy. http://www.jbc.org/content/early/2018/11/12/jbc.RA118.005914.abstract

p53 accumulation following cytokinesis failure in the absence of caspase-2 (letter) – Yoon Lim, Dylan De Bellis, Loretta Dorstyn and Sharad Kumar. https://www.nature.com/articles/s41418-018-0161-0

microRNA-378 promotes autophagy and inhibits apoptosis in skeletal muscle – Yan Li, Jingjing Jiang, Wei Liu, Hui Wang, Lei Zhao, Shengnan Liu, Peng Li, Shengjie Zhang, Chao Sun, Yuting Wu, Shuxian Yu, Xihua Li, Hui Zhang, Haifeng Qian, Duo Zhang, Feifan Guo, Qiwei Zhai, Qiurong Ding, Li Wang and Hao Ying. http://www.pnas.org/content/115/46/E10849?etoc=

Platelet CD36 signaling through ERK5 promotes caspase-dependent procoagulant activity and fibrin deposition in vivo – Moua Yang, Andaleb Kholmukhamedov, Marie L. Schulte, Brian C. Cooley, Na’il O. Scoggins, Jeremy P. Wood, Scott J. Cameron, Craig N. Morrell, Shawn M. Jobeand Roy L. Silverstein. http://www.bloodadvances.org/content/2/21/2848.abstract?etoc


Necroptosis


Axonal degeneration induced by glutamate excitotoxicity is mediated by necroptosis – Diego E. Hernández, Natalia A. Salvadores, Guillermo Moya-Alvarado, Romina J. Catalán, Francisca C. Bronfman and Felipe A. Court. http://jcs.biologists.org/content/131/22/jcs214684?etoc

Soluble TNF-like weak inducer of apoptosis (TWEAK) enhances poly(I:C)-induced RIPK1-mediated necroptosis – Mohamed A. Anany, Jennifer Kreckel, Simone Füllsack, Alevtina Rosenthal, Christoph Otto, Daniela Siegmund and Harald Wajant. https://www.nature.com/articles/s41419-018-1137-1

hsa-miR-500a-3P alleviates kidney injury by targeting MLKL-mediated necroptosis in renal epithelial cells – Ling Jiang, Xue-Qi Liu, Qiuying Ma, Qin Yang, Li Gao, Hai-Di Li, Jia-Nan Wang, Biao Wei, Jiagen Wen, Jun Li, Yong-Gui Wu and Xiao-Ming Meng. https://www.fasebj.org/doi/abs/10.1096/fj.201801711R?ai=ts&ui=ly8&af=T


Miscellanous


The Proton-Coupled Monocarboxylate Transporter Hermes Is Necessary for Autophagy during Cell Death – Panagiotis D. Velentzas, Lejie Zhang, Gautam Das, Tsun-Kai Chang, Charles Nelson, William R. Kobertz, Eric H. Baehrecke. https://www.cell.com/developmental-cell/fulltext/S1534-5807(18)30744-5

Intracellular transport is accelerated in early apoptotic cells – Bo Li, Shuo-Xing Dou, Jing-Wen Yuan, Yu-Ru Liu, Wei Li, Fangfu Ye, Peng-Ye Wang and Hui Li. http://www.pnas.org.sire.ub.edu/content/115/48/12118?etoc=

The yeast mitochondrial permeability transition is regulated by reactive oxygen species, endogenous Ca2+ and Cpr3, mediating cell death – Yoshiko Kamei, Masami Koushi, Yasunori Aoyama, Rei Asakai. https://www.sciencedirect.com/science/article/pii/S000527281830197X

microRNAs selectively protect hub cells of the germline stem cell niche from apoptosis – Marina Volin, Maayan Zohar-Fux, Oren Gonen, Lilach Porat-Kuperstein and Hila Toledano. http://jcb.rupress.org/content/217/11/3829?etoc


Reviews


FLIP as a therapeutic target in cancer – Luke Humphreys, Margarita Espona‐Fiedler, Daniel B. Longley. https://febs.onlinelibrary.wiley.com/doi/10.1111/febs.14523

Counting on Death – Quantitative aspects of Bcl‐2 family regulation – Annika Hantusch, Markus Rehm, Thomas Brunner. https://febs.onlinelibrary.wiley.com/doi/10.1111/febs.14516

Cell-in-cell phenomena in cancer – Stefano Fais and Michael Overholtzer. https://www.nature.com/articles/s41568-018-0073-9

FADD at the Crossroads between Cancer and Inflammation – Sara Mouasni, Léa Tourneur. https://www.cell.com/trends/immunology/fulltext/S1471-4906(18)30189-3

Hematologic Tumor Cell Resistance to the BCL-2 Inhibitor Venetoclax: A Product of Its Microenvironment? – Joel D. Leverson and Dan Cojocari. https://www.frontiersin.org/articles/10.3389/fonc.2018.00458/full

Dependence receptors – the dark side awakens – Ana‐Maria Negulescu, Patrick Mehlen. https://febs.onlinelibrary.wiley.com/doi/10.1111/febs.14507


Comments


Unleashing Blocked Apoptosis in Cancer Cells: New MCL1 Inhibitors Find Their Groove – Brian Leber, Justin Kale and David W. Andrews. http://cancerdiscovery.aacrjournals.org/content/8/12/1511?

TBK1 and IKKε restrain cell death – Klaus Heger and Vishva M. Dixit. https://www.nature.com/articles/s41556-018-0239-4

Timed degradation of Mcl-1 controls mitotic cell death – Paul R. Clarke, Lindsey A. Allan and Agnieszka Skowyra. https://www.tandfonline.com/doi/full/10.1080/23723556.2018.1516450

Necroptosis is key to axonal degeneration after excitotoxicity. http://jcs.biologists.org/content/131/22/e2202?etoc

Apolist – december 09

BH3

Glycolysis inhibition sensitizes tumor cells to death receptors-induced apoptosis by AMP kinase activation leading to Mcl-1 block in translation.
Pradelli LA, Bénéteau M, Chauvin C, Jacquin MA, Marchetti S, Muñoz-Pinedo C, Auberger P, Pende M, Ricci JE.
http://www.nature.com/onc/journal/vaop/ncurrent/full/onc2009448a.html

Caspase-independent Mitochondrial Cell Death Results from Loss of Respiration, Not Cytotoxic Protein Release
Lydia Lartigue, Yulia Kushnareva, Youngmo Seong, Helen Lin, Benjamin Faustin, and Donald D. Newmeyer
http://www.molbiolcell.org/cgi/content/abstract/20/23/4871?etoc

Single-cell quantification of Bax activation and mathematical modelling suggest pore formation on minimal mitochondrial Bax accumulation
HDüssmann, M Rehm, C G Concannon, S Anguissola, M Würstle, S Kacmar, P Völler, H J Huber and J H M Prehn
http://www.nature.com/cdd/journal/vaop/ncurrent/full/cdd2009123a.html

Functional Cooperation of the Proapoptotic Bcl2 Family Proteins Bmf and Bim In Vivo
Anette Hübner, Julie Cavanagh-Kyros, Mercedes Rincon, Richard A. Flavell, and Roger J. Davis
Mol. Cell. Biol. 2010;30 98-105
http://mcb.asm.org/cgi/content/abstract/30/1/98

Identification of proapoptotic Bim as a tumor suppressor in neoplastic mast cells: role of KIT D816V and effects of various targeted drugs
Karl J. Aichberger, Karoline V. Gleixner, Irina Mirkina, Sabine Cerny-Reiterer, Barbara Peter, Veronika Ferenc, Michael Kneidinger, Christian Baumgartner, Matthias Mayerhofer, Alexander Gruze, Winfried F. Pickl, Christian Sillaber, and Peter Valent
Blood 2009;114 5342-5351
http://bloodjournal.hematologylibrary.org/cgi/content/abstract/114/26/5342

VDAC2 is required for truncated BID-induced mitochondrial apoptosis by recruiting BAK to the mitochondria
Soumya Sinha Roy, Amy M Ehrlich, William J Craigen and György Hajnóczky
http://www.nature.com/embor/journal/v10/n12/abs/embor2009219.html

Voltage-dependent anion channel-1-based peptides interact with Bcl2 to prevent anti-apoptotic activity
Nir Arbel and Varda Shoshan-Barmatz
J. Biol. Chem. published 26 December 2009, 10.1074/jbc.M109.082990
http://www.jbc.org/cgi/content/abstract/M109.082990v1

Molecular details of Bax activation, oligomerization and membrane insertion
Stephanie Bleicken, Mirjam Classen, Pulagam V. L. Padmavathi, Takashi Ishikawa, Kornelius Zeth, Heinz-Jüergen Steinhoff, and Enrica Bordignon
J. Biol. Chem. published 13 December 2009, 10.1074/jbc.M109.081539
http://www.jbc.org/cgi/content/abstract/M109.081539v2

Vaccinia virus F1L interacts with Bak using highly divergent BCL-2 homology domains and replaces the function of Mcl-1
Stephanie Campbell, Bart Hazes, Marc Kvansakul, Peter Colman, and Michele Barry
J. Biol. Chem. published 2 December 2009, 10.1074/jbc.M109.053769
http://www.jbc.org/cgi/content/abstract/M109.053769v1

Bcl-xL changes conformation upon binding to wild-type but not mutant p53 DNA binding domain
Franz Hagn, Christian Klein, Oliver Demmer, Natasha Marchenko, Angelina Vaseva, Ute M. Moll, and Horst Kessler
J. Biol. Chem. published 2 December 2009, 10.1074/jbc.M109.065391
http://www.jbc.org/cgi/content/abstract/M109.065391v1
 

Death receptors and IAPs

Recruitment of the Linear Ubiquitin Chain Assembly Complex Stabilizes the TNF-R1 Signaling Complex and Is Required for TNF-Mediated Gene Induction
T.L. Haas, C.H. Emmerich, B. Gerlach, A.C. Schmukle, S.M. Cordier, E. Rieser, R. Feltham, J. Vince, U. Warnken, T. Wenger, R. Koschny, D. Komander, J. Silke, and H. Walczak
http://www.cell.com/molecular-cell/abstract/S1097-2765%2809%2900778-3

RIPK1 is not essential for TNFR1-induced activation of NF-B
W W-LWong, I E Gentle, U Nachbur, H Anderton, D L Vaux and J Silke
http://www.nature.com/cdd/journal/vaop/ncurrent/full/cdd2009178a.html

Cellular IAPs inhibit a cryptic CD95-induced cell death by limiting RIP1 kinase recruitment
Peter Geserick, Mike Hupe, Maryline Moulin, W. Wei-Lynn Wong, Maria Feoktistova, Beate Kellert, Harald Gollnick, John Silke, and Martin Leverkus
http://jcb.rupress.org/cgi/content/abstract/187/7/1037?etoc

Identification of an Xiap-Like Pseudogene on Mouse Chromosome 7
Aneta Kotevski, Wendy D. Cook, David L. Vaux, Bernard A. Callus
http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0008078

Modulation of Wnt signaling by the nuclear localization of cellular FLIP-L
Ryohei Katayama, Toshiyasu Ishioka, Shinji Takada, Ritsuko Takada, Naoya Fujita, Takashi Tsuruo, and Mikihiko Naito
J Cell Sci 2010;123 23-28
http://jcs.biologists.org/cgi/content/abstract/123/1/23

A Model of Partnership Co-Opted by the Homeodomain Protein TGIF and the Itch/AIP4 Ubiquitin Ligase for Effective Execution of TNF-α Cytotoxicity
C. Demange, N. Ferrand, C. Prunier, M.-F. Bourgeade, and A. Atfi
http://www.cell.com/molecular-cell/abstract/S1097-2765%2809%2900913-7
 

Caspases and downstream

Vaccinia Virus protein F1L is a caspase-9 inhibitor
Dayong Y. Zhai, Eric Yu, Chaofang Jin, Kate Welsh, Chung-wei Shiau, Lili Chen, Guy S. Salvesen, Robert Liddington, and John C. Reed
J. Biol. Chem. published 18 December 2009, 10.1074/jbc.M109.078113
http://www.jbc.org/cgi/content/abstract/M109.078113v1

Pretaporter, a Drosophila protein serving as a ligand for Draper in the phagocytosis of apoptotic cells
Takayuki Kuraishi, Yukiko Nakagawa, Kaz Nagaosa, Yumi Hashimoto, Takashi Ishimoto, Takeshi Moki, Yu Fujita, Hiroshi Nakayama, Naoshi Dohmae, Akiko Shiratsuchi, Naoko Yamamoto, Koichi Ueda, Masamitsu Yamaguchi, Takeshi Awasaki and Yoshinobu Nakanishi
http://www.nature.com/emboj/journal/v28/n24/abs/emboj2009343a.html

Annexin-II, DNA and histones serve as Factor H ligands on the surface of apoptotic cells
Jonatan Leffler, Andrew P. Herbert, Eva Norstrom, Chistoph Q. Schmidt, Paul N. Barlow, Anna M. Blom, and Myriam Martin
J. Biol. Chem. published 1 December 2009, 10.1074/jbc.M109.045427
http://www.jbc.org/cgi/content/abstract/M109.045427v1

 
Other

Inhibition of the ER Ca2+ pump forces multidrug-resistant cells deficient in Bak and Bax into necrosis
Katja Janssen, Sibylle Horn, Mathis T. Niemann, Peter T. Daniel, Klaus Schulze-Osthoff, and Ute Fischer
J Cell Sci 2009;122 4481-4491
http://jcs.biologists.org/cgi/content/abstract/122/24/4481

Yeast acetic acid-induced programmed cell death can occur without cytochrome c release which requires metacaspase YCA1
Nicoletta Guaragnella, Antonella Bobba, Salvatore Passarella, Ersilia Marra, Sergio Giannattasio
http://dx.doi.org/10.1016/j.febslet.2009.11.072
 
REVIEWS

A Tangled Web of Ubiquitin Chains: Breaking News in TNF-R1 Signaling
K. Bianchi and P. Meier
http://www.cell.com/molecular-cell/abstract/S1097-2765%2809%2900870-3

Mitochondrial cell death effectors
Dirk Brenner, Tak W Mak
http://dx.doi.org/10.1016/j.ceb.2009.09.009

Regulation of cell death by the ubiquitin–proteasome system
Maya Bader, Hermann Steller
http://dx.doi.org/10.1016/j.ceb.2009.09.005

Glucose metabolism and programmed cell death: an evolutionary and mechanistic perspective
Ayala King, Eyal Gottlieb
http://dx.doi.org/10.1016/j.ceb.2009.09.009

Caspase substrates: easily caught in deep waters?
Dieter Demon1, Petra Van Damme, Tom Vanden Berghe, Joël Vandekerckhove, Wim Declercq, Kris Gevaert and Peter Vandenabeele
http://dx.doi.org/10.1016/j.tibtech.2009.09.007

CDD: Special Issue on The Ubiquitin Proteasome System
http://www.nature.com/cdd/index.html

Including:

Regulation of TNFRSF and innate immune signalling complexes by TRAFs and cIAPs
J Silke and R Brink
http://www.nature.com/cdd/journal/v17/n1/full/cdd2009114a.html

The role of ubiquitylation for the control of cell death in Drosophila
A Bergmann
http://www.nature.com/cdd/journal/v17/n1/full/cdd200970a.html

 
COMMENTS

ER stress: another route to cell death
J Cell Sci 2009;122 e2401
http://jcs.biologists.org/cgi/content/full/122/24/e2401

Apoptosis: it’s BAK to VDAC
Gordon C. Shore
http://www.nature.com/embor/journal/v10/n12/full/embor2009249.html



Apolist – november 09

REVIEWS
.
Emerging Role for Members of the Bcl-2 Family in Mitochondrial Morphogenesis
A. Autret and S.J. Martin
http://dx.doi.org/10.1016/j.molcel.2009.10.011
.

Novel roles for GAPDH in cell death and carcinogenesis

A Colell, D R Green and J-E Ricci

.

Cell Death
Richard S. Hotchkiss, M.D., Andreas Strasser, Ph.D., Jonathan E.
McDunn, Ph.D., and Paul E. Swanson, M.D.
http://content.nejm.org/cgi/content/full/361/16/1570


BH3

Bak Activation for Apoptosis Involves Oligomerization of Dimers via
Their α6 Helices
G. Dewson, T. Kratina, P. Czabotar, C.L. Day, J.M. Adams, and R.M. Kluck
http://www.cell.com/molecular-cell/abstract/S1097-2765(09)00821-1

Membrane promotes tBID interaction with BCL(XL).
García-Sáez AJ, Ries J, Orzáez M, Pérez-Payà E, Schwille P.
http://www.nature.com/nsmb/journal/v16/n11/abs/nsmb.1671.html

Stepwise Activation of BAX and BAK by tBID, BIM, and PUMA Initiates
Mitochondrial Apoptosis
H. Kim, H.-C. Tu, D. Ren, O. Takeuchi, J.R. Jeffers, G.P. Zambetti,
J.J.-D. Hsieh, and E.H.-Y. Cheng
http://www.cell.com/molecular-cell/abstract/S1097-2765(09)00690-X

Bax contains two functional mitochondrial targeting sequences and
translocates to mitochondria in a conformational change- and
homo-oligomerization-driven process
Nicholas M. George, Natalie Targy, Jacquelynn J. D. Evans, Liqiang
Zhang, and Xu Luo
http://www.jbc.org/cgi/content/abstract/M109.049924v1

Bim Upregulation by Histone Deacetylase Inhibitors Mediates
Interactions with the Bcl-2 Antagonist ABT-737: Evidence for Distinct
Roles for Bcl-2, Bcl-xL, and Mcl-1
Shuang Chen, Yun Dai, Xin-Yan Pei, and Steven Grant
http://mcb.asm.org/cgi/content/abstract/29/23/6149

The BH3-only protein Bim plays a critical role in leukemia cell death
triggered by concomitant inhibition of the PI3K/Akt and MEK/ERK1/2
pathways
Mohamed Rahmani, Anh Anderson, Joseph Reza Habibi, Timothy Ryan
Crabtree, Mandy Mayo, Hisashi Harada, Andrea Ferreira-Gonzalez, Paul
Dent, and Steven Grant
http://bloodjournal.hematologylibrary.org/cgi/content/abstract/114/20/4507

From the Cover: Age-related hearing loss in C57BL/6J mice is mediated
by Bak-dependent mitochondrial apoptosis
Shinichi Someya, Jinze Xu, Kenji Kondo, Dalian Ding, Richard J. Salvi,
Tatsuya Yamasoba, Peter S. Rabinovitch, Richard Weindruch, Christiaan
Leeuwenburgh, Masaru Tanokura, and Tomas A. Prolla
http://www.pnas.org/content/106/46/19432.abstract?etoc

Facilitation of mitochondrial outer and inner membrane
permeabilization and cell death in oxidative stress by a novel BH3
domain protein
A. Szigeti, E. Hocsak, E. Rapolti, B. Racz, A. Boronkai, E. Pozsgai,
B. Debreceni, Z. Bognar, S. Bellyei, B. Sumegi, and F. Gallyas, Jr.
http://www.jbc.org/cgi/content/abstract/M109.015222v1

Dissimilar mechanisms of cytochrome c release induced by octyl
glucoside-activated BAX and by BAX activated with truncated BID
Tsyregma Li, Tatiana Brustovetsky, Bruno Antonsson, Nickolay Brustovetsky
http://dx.doi.org/10.1016/j.bbabio.2009.07.012


Miscellaneous

Autophagy, Not Apoptosis, Is Essential for Midgut Cell Death in Drosophila
D. Denton, B. Shravage, R. Simin, K. Mills, D.L. Berry, E.H.
Baehrecke, and S. Kumar
http://dx.doi.org/10.1016/j.cub.2009.08.042

Determinism and divergence of apoptosis susceptibility in mammalian cells
Patrick D. Bhola and Sanford M. Simon
J Cell Sci 2009;122 4296-4302
http://jcs.biologists.org/cgi/content/abstract/122/23/4296

GM1-Ganglioside Accumulation at the Mitochondria-Associated ER
Membranes Links ER Stress to Ca2+-Dependent Mitochondrial Apoptosis
R. Sano, I. Annunziata, A. Patterson, S. Moshiach, E. Gomero, J.
Opferman, M. Forte, and A. d’Azzo
http://www.cell.com/molecular-cell/abstract/S1097-2765(09)00786-2

Granzyme F induces a novel death pathway characterized by
Bid-independent cytochrome c release without caspase activation
LShi, L Wu, S Wang and Z Fan
http://www.nature.com/cdd/journal/v16/n12/abs/cdd2009101a.html


IAPs and death receptors

CD95 engagement mediates actin-independent and -dependent apoptotic signals
BChaigne-Delalande, W Mahfouf, S Daburon, J-F Moreau and P Legembre
http://www.nature.com/cdd/journal/v16/n12/abs/cdd2009111a.html

PU.1 induces apoptosis in myeloma cells through direct transactivation of TRAIL
S Ueno, H Tatetsu, H Hata, T Iino, H Niiro, K Akashi, D G Tenen, H
Mitsuya and Y Okuno
http://www.nature.com/onc/journal/v28/n46/full/onc2009263a.html

A role for X-linked inhibitor of apoptosis protein upstream of
mitochondrial permeabilization
Thomas W. Owens, Fiona M. Foster, Anthony Valentijn, Andrew P.
Gilmore, and Charles H. Streuli
http://www.jbc.org/cgi/content/abstract/M109.072322v1


Caspases and downstream

PPAR-δ senses and orchestrates clearance of apoptotic cells to promote tolerance

Lata Mukundan, Justin I Odegaard, Christine R Morel, Jose E Heredia, Julia W Mwangi, Roberto R Ricardo-Gonzalez, Y P Sharon Goh, Alex Red Eagle, Shannon E Dunn, Jennifer U H Awakuni, Khoa D Nguyen, Lawrence Steinman, Sara A Michie and Ajay Chawl

http://www.nature.com/nm/journal/v15/n11/full/nm.2048.html

Recognition of apoptotic cells by epithelial cells: conserved versus
tissue-specific signaling responses
Vimal A. Patel, Daniel J. Lee, Lanfei Feng, Angelika Antoni, Wilfred
Lieberthal, John H. Schwartz, Joyce Rauch, David S. Ucker, and Jerrold
S. Levine
J. Biol. Chem. published 12 November 2009, 10.1074/jbc.M109.018440
http://www.jbc.org/cgi/content/abstract/M109.018440v1

Necrotic cells trigger a sterile inflammatory response through the
Nlrp3 inflammasome
Shankar S. Iyer, Wilco P. Pulskens, Jeffrey J. Sadler, Loes M. Butter,
Gwendoline J. Teske, Tyler K. Ulland, Stephanie C. Eisenbarth,
Sandrine Florquin, Richard A. Flavell, Jaklien C. Leemans, and Fayyaz
S. Sutterwala
http://www.pnas.org/content/106/48/20388.abstract?etoc


COMMENTS

BAX and BAK Caught in the Act
Y. Yao and F.M. Marassi
http://www.cell.com/molecular-cell/abstract/S1097-2765(09)00788-6

Apoptosis: the generation gap
http://jcs.biologists.org/cgi/content/full/122/23/e2302?etoc

Caspase 2 in apoptosis, the DNA damage response and tumour
suppression: enigma no more?
Sharad Kumar
http://www.nature.com/nrc/journal/v9/n12/full/nrc2745.html